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  • 1
    Electronic Resource
    Electronic Resource
    Sr2+ can become incorporated into an agonist-sensitive, cytoplasmic Ca2+ store in a cell line derived from the equine sweat gland epithelium (1995)
    Springer
    Cellular and molecular life sciences 51 (1995), S. 804-808 
    Details
    ISSN: 1420-9071
    Keywords: Ca2+ mobilisation ; purinergic receptors ; nucleotide receptors ; sweat gland ; epithelial cells ; ionomycin ; Fura-2 ; horse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We have explored the properties of a Ca2+-dependent cell-signalling pathway that becomes active when cultured equine sweat gland cells are stimulated with ATP. The ATP-regulated, Ca2+-influx pathway allowed Sr2+ to enter the cytoplasm but permitted only a minimal influx of Ba2+. Experiments in which cells were repeatedly stimulated with ATP suggested that Sr2+, but not Ba2+, could become incorporated into the agonist-sensitive, cytoplasmic Ca2+ store. Further evidence for this was provided by experiments using ionomycin, a Ca2+ ionophore which has no affinity for Sr2+.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01922434
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Mechanical properties of normal andmdx mouse sarcolemma: Bearing on function of dystrophin (1991)
    Springer
    Journal of muscle research and cell motility 12 (1991), S. 585-589 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The tensile strength of the muscle fibre surface membrane was estimated (1) from the suction required to burst membrane patches and (2) by aspiration of sarcolemmal vesicles into micropipettes of uniform bore. Each method gave an average value close to 60 μN cm−1 for the maximum tension sustainable by normal mouse sarcolemma and only slightly lower values for sarcolemma frommdx mice which lack dystrophin. The elastic modulus of area expansion, as measurable by pipette aspiration of sarcolemmal vesicles, was found to have an average value of 3160 μN cm−1 for normal and 2770 μN cm−1 formdx mouse sarcolemma. The tensile strength of the sarcolemma is much too small for any differences in it to be the basis for the different osmotic behaviour of normal andmdx muscle fibres reported recently (Menke & Jockusch, 1991). By analogy with the better understood origin of the osmotic fragility of different types of red blood cells, the higher osmotic fragility ofmdx muscle fibres is suggested to be of morphological origin. We postulate that dystrophin functions as an element of the submembrane cytoskeleton so as to maintain the normal folding which safeguards the sarcolemma against mechanical damage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01738447
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    Paper (German National Licenses)
    Fulltext
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